Slabas A R, Walker D A
Biochem J. 1976 Jan 15;154(1):185-92. doi: 10.1042/bj1540185.
ADP was shown to inhibit phosphoglycerate-dependent O2 evolution in a simplified reconstituted chloroplast system containing 3-phosphoglycerate kinase and triose phosphate dehydrogenase. Rates of O2 evolution in the simplified system are comparable with those obtained by using stromal protein rather than purified enzymes. ADP does not inhibit O2 evolution with glycerate 1,3-biphosphate as substrate nor does it inhibit triose phosphate dehydrogenase. The inhibitory effect of ADP is attributed to an increase in the rate of conversion of glycerate biphosphate into phosphoglycerate. The results are discussed in terms of control by ADP of phosphoglycerate-dependent oxygen evolution.
在含有3-磷酸甘油酸激酶和磷酸丙糖脱氢酶的简化重组叶绿体系统中,ADP被证明可抑制磷酸甘油酸依赖性的氧气释放。该简化系统中的氧气释放速率与使用基质蛋白而非纯化酶所获得的速率相当。以1,3-二磷酸甘油酸为底物时,ADP不会抑制氧气释放,它也不会抑制磷酸丙糖脱氢酶。ADP的抑制作用归因于二磷酸甘油酸向磷酸甘油酸转化速率的增加。就ADP对磷酸甘油酸依赖性氧气释放的控制作用对结果进行了讨论。